USP17, a ubiquitin specific enzyme, is responsible for the progression of the cell cycle to promote cellular proliferation. In many cancers, including breast and prostate, USP17 levels are upregulated, promoting unregulated proliferation and cancer. Over the last 10 years, cell-based studies have identified USP17 as a potential target for cancer therapy; however, there has been no advancement in the production of recombinant USP17. Availability of large amounts of purified, recombinant USP17 is critical for developing an anticancer therapeutic against this target.

Researchers from Purdue University have developed a methodology for the expression and purification of recombinant USP17, which allows for the utilization of a much wider array of techniques compared to cell based assays. Recombinant USP17 can be used for kinetic, structural, biochemical studies, and other studies of the enzyme and its response to drug candidates. The Purdue researchers' protocol and the resulting recombinant protein provide others with the tools to develop therapeutics against cancers in which USP17 regulation is a major component. This method will help advance the development of anticancer therapeutics that target USP17.